8vml

PRC2_AJ1-450 bound to H3K4me3

Method: ELECTRON MICROSCOPY Dmax: 158.9 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

SUZ12

Homo sapiens

UniProt Q15022

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–739 Not recorded JARID2 × 1 (Q92833) EZH2 × 1 (Q15910) Histone H3 × 1 (P68431) EED × 1 (O75530) RBAP48 × 1 (Q09028) AEPB2 × 1 (Q6ZN18) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

29 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUZ12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–739; UniProt 1–739

JARID2

Homo sapiens

UniProt Q92833

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–1246 Non-standard monomer:Yes (specific site not provided by mmCIF) SUZ12 × 1 (Q15022) EZH2 × 1 (Q15910) Histone H3 × 1 (P68431) EED × 1 (O75530) RBAP48 × 1 (Q09028) AEPB2 × 1 (Q6ZN18) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name JARD2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1246; UniProt 1–1246

EZH2

Homo sapiens

UniProt Q15910

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–746 Not recorded SUZ12 × 1 (Q15022) JARID2 × 1 (Q92833) Histone H3 × 1 (P68431) EED × 1 (O75530) RBAP48 × 1 (Q09028) AEPB2 × 1 (Q6ZN18) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

35 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EZH2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–746; UniProt 1–746

Histone H3

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain I; UniProt 20–41 Not recorded SUZ12 × 1 (Q15022) JARID2 × 1 (Q92833) EZH2 × 1 (Q15910) EED × 1 (O75530) RBAP48 × 1 (Q09028) AEPB2 × 1 (Q6ZN18) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain I; PDBConstruct 1–22; UniProt 20–41

EED

Homo sapiens

UniProt O75530

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain L; UniProt 1–441 Not recorded SUZ12 × 1 (Q15022) JARID2 × 1 (Q92833) EZH2 × 1 (Q15910) Histone H3 × 1 (P68431) RBAP48 × 1 (Q09028) AEPB2 × 1 (Q6ZN18) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

77 other PDB entries and 112 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EED_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–441; UniProt 1–441

RBAP48

Homo sapiens

UniProt Q09028

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain N; UniProt 1–425 Not recorded SUZ12 × 1 (Q15022) JARID2 × 1 (Q92833) EZH2 × 1 (Q15910) Histone H3 × 1 (P68431) EED × 1 (O75530) AEPB2 × 1 (Q6ZN18) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

49 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBBP4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain N; PDBConstruct 1–425; UniProt 1–425

AEPB2

Homo sapiens

UniProt Q6ZN18

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain P; UniProt 1–301 Not recorded SUZ12 × 1 (Q15022) JARID2 × 1 (Q92833) EZH2 × 1 (Q15910) Histone H3 × 1 (P68431) EED × 1 (O75530) RBAP48 × 1 (Q09028) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

17 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AEBP2_HUMAN
Isoform Q6ZN18-3
PDB entities 7
Chains and sequence ranges Author chain P; PDBConstruct 1–301; UniProt 1–301

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8vml

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vml
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vml
Deposition date deposition_date2024-01-13
Structure title titlePRC2_AJ1-450 bound to H3K4me3
Keywords keywordscomplex, methyltransferase, histone, epigenetics, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.21
Radius of gyration Rg (electron density) rg_electron44.91
Forward intensity I(0) i0693078000.00
Molecular weight molecular_weight212020.0 kDa
Excluded volume excluded_volume263140 ų
Envelope volume envelope_volume398190 ų
Hydration-shell volume shell_volume73556 ų
Envelope diameter envelope_diameter170.2
Shell Rg shell_rg49.44
Envelope Rg envelope_rg45.04
Shape Rg shape_rg44.94
Total Rg total_rg45.02
Total atoms total_atoms14947
Residues n_residues1991
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax158.9
Rg (real space) rg_real45.26
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real6.9310e+08
I(0) uncertainty (real space) i0_real_error1.2130e+07
Rg (reciprocal space) rg_reciprocal45.21
I(0) (reciprocal space) i0_reciprocal693000000.0000
Solution quality estimate total_estimate0.8673
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.5
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.206
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha136000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)